ID A0A7T6Z7T9_9BACI Unreviewed; 690 AA. AC A0A7T6Z7T9; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 08-NOV-2023, entry version 9. DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458}; DE EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458}; GN Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458}; GN ORFNames=HUG20_00525 {ECO:0000313|EMBL:QQK78555.1}; OS Salicibibacter cibi. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salicibibacter. OX NCBI_TaxID=2743001 {ECO:0000313|EMBL:QQK78555.1, ECO:0000313|Proteomes:UP000595349}; RN [1] {ECO:0000313|EMBL:QQK78555.1, ECO:0000313|Proteomes:UP000595349} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NKC21-4 {ECO:0000313|EMBL:QQK78555.1, RC ECO:0000313|Proteomes:UP000595349}; RA Oh Y.J.; RT "Genomic analysis of Salicibibacter sp. NKC21-4."; RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for CC both cytoplasmic and membrane proteins. Plays a role in the quality CC control of integral membrane proteins. {ECO:0000256|HAMAP- CC Rule:MF_01458}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01458}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01458}; CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01458}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. CC {ECO:0000256|RuleBase:RU003651}. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41 CC family. {ECO:0000256|ARBA:ARBA00010044, ECO:0000256|HAMAP- CC Rule:MF_01458}. CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family. CC {ECO:0000256|HAMAP-Rule:MF_01458}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP054706; QQK78555.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7T6Z7T9; -. DR KEGG; scib:HUG20_00525; -. DR Proteomes; UP000595349; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd19501; RecA-like_FtsH; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.20.58.760; Peptidase M41; 1. DR HAMAP; MF_01458; FtsH; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR005936; FtsH. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000642; Peptidase_M41. DR InterPro; IPR037219; Peptidase_M41-like. DR NCBIfam; TIGR01241; FtsH_fam; 1. DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1. DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF17862; AAA_lid_3; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF140990; FtsH protease domain-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00674; AAA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01458}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP- KW Rule:MF_01458}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01458}. FT TRANSMEM 7..26 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT TRANSMEM 117..138 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 202..341 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 615..690 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 632..668 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 433 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 210..217 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 432 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 436 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 508 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 690 AA; 76489 MW; FB88756CDCBE4CA0 CRC64; MNRTVRYTFF WLFVLLILIG IVQLFTDDPV EDEMMNTDEF MQALEQDEIA SMTVQPEMEV YLIEGEMVNG GEEDEANEFT AHILRSPEVT DMLLDAMETN ESLTAVDTEP GEEPGGWLQF LVAVIPFIII FILFFFLLSQ MQGGGNKMMN FGKSKAKMQQ ESDKKKARFK DVAGAEEEKQ ELVEIVDFLK DPRKFANIGA RIPKGVLLVG PPGTGKTLLG RAVAGEAGVP FFSISGSDFV EMFVGVGASR VRDLFNNAKN NAPCIIFIDE LDAVGRQRGA GVGGGHDERE QTLNQLLVEM DGFEGNEGII IIAATNRSDV LDPALLRPGR FDRQITVGLP DVRGREDVLK VHVREKPIDD DVELGAIAQR TPGFSGAELE NLLNEAALVA ARSNSVKIKM VHIEEAIDRV IAGPAKKTRV ISEKEKNIVA HHEAGHTVVG VKLQNADAVH KVTIVPRGQA GGYAMMLPKE DRYFMTKPEL LDKIVGLLGG RVSEDIIFGE ASTGAHNDFQ RATAIARKMV MEYGMSEKLG PLQFGSTGGG QVFLGRDIQN EQNYSDAIAH EIDKEVQKII KDSYERCRQI LTENKDKLEL VAQNLLELET LDAEQIYSLV EEGKLPEGHH SNQTQEDALK NSGDVDPVDD ENVKVNIGSQ EEEQPETKND QSKANEETEE QDQTEEQDNE EKQEDDNRRS //